| content |
HEADER HYDROLASE 28-OCT-10 3PF8
TITLE CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL ESTERASE
TITLE 2 LJ0536
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CINNAMOYL ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS JOHNSONII;
SOURCE 3 ORGANISM_TAXID: 33959;
SOURCE 4 GENE: LJ0536;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P15TV-L
KEYWDS ALPHA/BETA HYDROLASE FOLD, ESTERASE, HYDROLASE, CINNAMOYL/FERULOYL
KEYWDS 2 ESTERASE, HYDROXYCINAMMATES, EXTRACELLULAR
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,K.K.LAI,C.VU,X.XU,H.CUI,S.MOLLOY,C.F.GONZALEZ,A.YAKUNIN,
AUTHOR 2 A.SAVCHENKO
REVDAT 1 31-AUG-11 3PF8 0
JRNL AUTH K.K.LAI,P.J.STOGIOS,C.VU,X.XU,H.CUI,S.MOLLOY,A.SAVCHENKO,
JRNL AUTH 2 A.YAKUNIN,C.F.GONZALEZ
JRNL TITL AN INSERTED ALPHA/BETA SUBDOMAIN SHAPES THE CATALYTIC POCKET
JRNL TITL 2 OF LACTOBACILLUS JOHNSONII CINNAMOYL ESTERASE
JRNL REF PLOS ONE V. 6 2011
JRNL REFN ESSN 1932-6203
JRNL DOI 10.1371/JOURNAL.PONE.0023269
REMARK 2
REMARK 2 RESOLUTION. 2.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.8.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 23386
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1194
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2646
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2781
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2506
REMARK 3 BIN R VALUE (WORKING SET) : 0.2733
REMARK 3 BIN FREE R VALUE : 0.3654
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.29
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 140
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3836
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 146
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.50930
REMARK 3 B22 (A**2) : 0.50930
REMARK 3 B33 (A**2) : -1.01870
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.40
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.918
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.838
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3912 ; 2.000 ; NULL
REMARK 3 BOND ANGLES : 5320 ; 2.000 ; NULL
REMARK 3 TORSION ANGLES : 1332 ; 2.000 ; NULL
REMARK 3 TRIGONAL CARBON PLANES : 116 ; 2.000 ; NULL
REMARK 3 GENERAL PLANES : 569 ; 5.000 ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : 3912 ; 20.000 ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 524 ; 5.000 ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4663 ; 4.000 ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.23
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.49
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 21.54
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: A -5 A 179
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7143 17.1511 35.6343
REMARK 3 T TENSOR
REMARK 3 T11: -0.0106 T22: 0.1122
REMARK 3 T33: -0.2379 T12: 0.0000
REMARK 3 T13: 0.0178 T23: -0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 1.1062 L22: 1.4455
REMARK 3 L33: 1.1853 L12: -0.1858
REMARK 3 L13: 0.2373 L23: -0.2226
REMARK 3 S TENSOR
REMARK 3 S11: -0.0338 S12: 0.1592 S13: -0.1093
REMARK 3 S21: 0.0846 S22: 0.0579 S23: -0.2176
REMARK 3 S31: -0.0076 S32: 0.1150 S33: -0.0241
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: A 180 A 245
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6845 10.8046 48.2312
REMARK 3 T TENSOR
REMARK 3 T11: 0.0441 T22: 0.1849
REMARK 3 T33: -0.2314 T12: 0.0406
REMARK 3 T13: 0.0314 T23: 0.0513
REMARK 3 L TENSOR
REMARK 3 L11: 0.5169 L22: 1.7611
REMARK 3 L33: 0.7990 L12: -0.9561
REMARK 3 L13: 0.2162 L23: -0.7810
REMARK 3 S TENSOR
REMARK 3 S11: -0.0660 S12: -0.0749 S13: -0.2366
REMARK 3 S21: 0.2453 S22: 0.0479 S23: 0.0699
REMARK 3 S31: -0.0476 S32: -0.1825 S33: 0.0181
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: B 2 B 179
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7076 29.8159 15.1326
REMARK 3 T TENSOR
REMARK 3 T11: 0.1115 T22: 0.1228
REMARK 3 T33: -0.2648 T12: -0.0805
REMARK 3 T13: -0.0205 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 0.3612 L22: 2.0174
REMARK 3 L33: 0.1388 L12: -0.2897
REMARK 3 L13: 0.1518 L23: -0.7242
REMARK 3 S TENSOR
REMARK 3 S11: -0.0650 S12: 0.1021 S13: 0.0654
REMARK 3 S21: -0.3238 S22: 0.1038 S23: 0.0926
REMARK 3 S31: -0.0102 S32: 0.0419 S33: -0.0388
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: B 180 B 245
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8958 33.3697 12.4356
REMARK 3 T TENSOR
REMARK 3 T11: 0.0789 T22: 0.0599
REMARK 3 T33: -0.1350 T12: -0.0532
REMARK 3 T13: -0.0923 T23: 0.1222
REMARK 3 L TENSOR
REMARK 3 L11: 0.1741 L22: 0.7084
REMARK 3 L33: 0.0015 L12: -0.2960
REMARK 3 L13: 0.4070 L23: 0.1701
REMARK 3 S TENSOR
REMARK 3 S11: 0.0086 S12: 0.0840 S13: -0.0584
REMARK 3 S21: -0.1288 S22: 0.0502 S23: 0.4516
REMARK 3 S31: 0.1690 S32: -0.0646 S33: -0.0587
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3PF8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB062305.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23389
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10500
REMARK 200 FOR THE DATA SET : 13.4400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.44200
REMARK 200 FOR SHELL : 4.810
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB CODE 2WTN POLY-ALANINE MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6, 20% PEG10K, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 74.94950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.27211
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 43.43633
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 74.94950
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 43.27211
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 43.43633
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 74.94950
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 43.27211
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 43.43633
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 74.94950
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 43.27211
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 43.43633
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 74.94950
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 43.27211
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 43.43633
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 74.94950
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 43.27211
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 43.43633
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 86.54423
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 86.87267
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 86.54423
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 86.87267
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 86.54423
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 86.87267
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 86.54423
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 86.87267
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 86.54423
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 86.87267
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 86.54423
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 86.87267
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 465 ASN A 246
REMARK 465 ASN A 247
REMARK 465 ALA A 248
REMARK 465 PHE A 249
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 ARG B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 ASN B 246
REMARK 465 ASN B 247
REMARK 465 ALA B 248
REMARK 465 PHE B 249
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A -4 CG CD1 CD2
REMARK 470 TYR A -3 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE A -2 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A -1 CG CD OE1 NE2
REMARK 470 LEU A 135 CG CD1 CD2
REMARK 470 ASP A 229 CG OD1 OD2
REMARK 470 LYS B 161 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 9 57.94 34.23
REMARK 500 PRO A 20 -151.87 -92.28
REMARK 500 ALA A 36 -162.33 -104.12
REMARK 500 ARG A 98 -82.51 -76.32
REMARK 500 SER A 106 -113.57 52.31
REMARK 500 ALA A 130 60.71 38.40
REMARK 500 LEU A 135 -32.81 -39.84
REMARK 500 ASN A 143 97.11 -163.11
REMARK 500 PHE A 160 -164.47 -114.83
REMARK 500 LEU A 163 -163.57 -115.59
REMARK 500 ALA A 183 -15.61 -48.65
REMARK 500 PHE A 227 100.73 -57.48
REMARK 500 ASP A 229 -123.10 63.36
REMARK 500 THR B 35 -0.39 75.90
REMARK 500 ASN B 39 70.04 -106.41
REMARK 500 ARG B 98 -73.41 -103.94
REMARK 500 SER B 106 -125.98 56.14
REMARK 500 ALA B 130 62.86 33.16
REMARK 500 ALA B 132 38.77 -68.39
REMARK 500 LYS B 161 -102.65 53.50
REMARK 500 CYS B 226 30.39 -80.33
REMARK 500 PHE B 227 57.17 33.12
REMARK 500 ASP B 229 -118.10 52.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 97 24.4 L L OUTSIDE RANGE
REMARK 500 THR B 35 23.5 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 251
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PF9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL
REMARK 900 ESTERASE LJ0536 S106A MUTANT
REMARK 900 RELATED ID: 3PFA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL
REMARK 900 ESTERASE LJ0536 S106A MUTANT IN COMPLEX WITH CAFFEIC ACID
REMARK 900 RELATED ID: 3PFB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL
REMARK 900 ESTERASE LJ0536 S106A MUTANT IN COMPLEX WITH ETHYLFERULATE
REMARK 900 RELATED ID: 3PFC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL
REMARK 900 ESTERASE LJ0536 S106A MUTANT IN COMPLEX WITH FERULIC ACID
DBREF 3PF8 A 1 249 UNP D3YEX6 D3YEX6_LACJO 1 249
DBREF 3PF8 B 1 249 UNP D3YEX6 D3YEX6_LACJO 1 249
SEQADV 3PF8 MET A -20 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 GLY A -19 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 SER A -18 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 SER A -17 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 HIS A -16 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 HIS A -15 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 HIS A -14 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 HIS A -13 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 HIS A -12 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 HIS A -11 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 SER A -10 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 SER A -9 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 GLY A -8 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 ARG A -7 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 GLU A -6 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 ASN A -5 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 LEU A -4 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 TYR A -3 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 PHE A -2 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 GLN A -1 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 GLY A 0 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 MET B -20 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 GLY B -19 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 SER B -18 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 SER B -17 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 HIS B -16 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 HIS B -15 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 HIS B -14 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 HIS B -13 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 HIS B -12 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 HIS B -11 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 SER B -10 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 SER B -9 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 GLY B -8 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 ARG B -7 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 GLU B -6 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 ASN B -5 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 LEU B -4 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 TYR B -3 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 PHE B -2 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 GLN B -1 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF8 GLY B 0 UNP D3YEX6 EXPRESSION TAG
SEQRES 1 A 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 270 ARG GLU ASN LEU TYR PHE GLN GLY MET ALA THR ILE THR
SEQRES 3 A 270 LEU GLU ARG ASP GLY LEU GLN LEU VAL GLY THR ARG GLU
SEQRES 4 A 270 GLU PRO PHE GLY GLU ILE TYR ASP MET ALA ILE ILE PHE
SEQRES 5 A 270 HIS GLY PHE THR ALA ASN ARG ASN THR SER LEU LEU ARG
SEQRES 6 A 270 GLU ILE ALA ASN SER LEU ARG ASP GLU ASN ILE ALA SER
SEQRES 7 A 270 VAL ARG PHE ASP PHE ASN GLY HIS GLY ASP SER ASP GLY
SEQRES 8 A 270 LYS PHE GLU ASN MET THR VAL LEU ASN GLU ILE GLU ASP
SEQRES 9 A 270 ALA ASN ALA ILE LEU ASN TYR VAL LYS THR ASP PRO HIS
SEQRES 10 A 270 VAL ARG ASN ILE TYR LEU VAL GLY HIS SER GLN GLY GLY
SEQRES 11 A 270 VAL VAL ALA SER MET LEU ALA GLY LEU TYR PRO ASP LEU
SEQRES 12 A 270 ILE LYS LYS VAL VAL LEU LEU ALA PRO ALA ALA THR LEU
SEQRES 13 A 270 LYS GLY ASP ALA LEU GLU GLY ASN THR GLN GLY VAL THR
SEQRES 14 A 270 TYR ASN PRO ASP HIS ILE PRO ASP ARG LEU PRO PHE LYS
SEQRES 15 A 270 ASP LEU THR LEU GLY GLY PHE TYR LEU ARG ILE ALA GLN
SEQRES 16 A 270 GLN LEU PRO ILE TYR GLU VAL SER ALA GLN PHE THR LYS
SEQRES 17 A 270 PRO VAL CYS LEU ILE HIS GLY THR ASP ASP THR VAL VAL
SEQRES 18 A 270 SER PRO ASN ALA SER LYS LYS TYR ASP GLN ILE TYR GLN
SEQRES 19 A 270 ASN SER THR LEU HIS LEU ILE GLU GLY ALA ASP HIS CYS
SEQRES 20 A 270 PHE SER ASP SER TYR GLN LYS ASN ALA VAL ASN LEU THR
SEQRES 21 A 270 THR ASP PHE LEU GLN ASN ASN ASN ALA PHE
SEQRES 1 B 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 270 ARG GLU ASN LEU TYR PHE GLN GLY MET ALA THR ILE THR
SEQRES 3 B 270 LEU GLU ARG ASP GLY LEU GLN LEU VAL GLY THR ARG GLU
SEQRES 4 B 270 GLU PRO PHE GLY GLU ILE TYR ASP MET ALA ILE ILE PHE
SEQRES 5 B 270 HIS GLY PHE THR ALA ASN ARG ASN THR SER LEU LEU ARG
SEQRES 6 B 270 GLU ILE ALA ASN SER LEU ARG ASP GLU ASN ILE ALA SER
SEQRES 7 B 270 VAL ARG PHE ASP PHE ASN GLY HIS GLY ASP SER ASP GLY
SEQRES 8 B 270 LYS PHE GLU ASN MET THR VAL LEU ASN GLU ILE GLU ASP
SEQRES 9 B 270 ALA ASN ALA ILE LEU ASN TYR VAL LYS THR ASP PRO HIS
SEQRES 10 B 270 VAL ARG ASN ILE TYR LEU VAL GLY HIS SER GLN GLY GLY
SEQRES 11 B 270 VAL VAL ALA SER MET LEU ALA GLY LEU TYR PRO ASP LEU
SEQRES 12 B 270 ILE LYS LYS VAL VAL LEU LEU ALA PRO ALA ALA THR LEU
SEQRES 13 B 270 LYS GLY ASP ALA LEU GLU GLY ASN THR GLN GLY VAL THR
SEQRES 14 B 270 TYR ASN PRO ASP HIS ILE PRO ASP ARG LEU PRO PHE LYS
SEQRES 15 B 270 ASP LEU THR LEU GLY GLY PHE TYR LEU ARG ILE ALA GLN
SEQRES 16 B 270 GLN LEU PRO ILE TYR GLU VAL SER ALA GLN PHE THR LYS
SEQRES 17 B 270 PRO VAL CYS LEU ILE HIS GLY THR ASP ASP THR VAL VAL
SEQRES 18 B 270 SER PRO ASN ALA SER LYS LYS TYR ASP GLN ILE TYR GLN
SEQRES 19 B 270 ASN SER THR LEU HIS LEU ILE GLU GLY ALA ASP HIS CYS
SEQRES 20 B 270 PHE SER ASP SER TYR GLN LYS ASN ALA VAL ASN LEU THR
SEQRES 21 B 270 THR ASP PHE LEU GLN ASN ASN ASN ALA PHE
HET NA A 250 1
HET NA B 250 1
HET NA B 251 1
HETNAM NA SODIUM ION
FORMUL 3 NA 3(NA 1+)
FORMUL 6 HOH *146(H2 O)
HELIX 1 1 THR A 40 ASP A 52 1 13
HELIX 2 2 LYS A 71 MET A 75 5 5
HELIX 3 3 VAL A 77 LYS A 92 1 16
HELIX 4 4 GLN A 107 TYR A 119 1 13
HELIX 5 5 THR A 134 GLY A 142 1 9
HELIX 6 6 GLY A 167 GLN A 174 1 8
HELIX 7 7 PRO A 177 ALA A 183 1 7
HELIX 8 8 PRO A 202 TYR A 212 1 11
HELIX 9 9 SER A 228 SER A 230 5 3
HELIX 10 10 TYR A 231 LEU A 243 1 13
HELIX 11 11 THR B 40 GLU B 53 1 14
HELIX 12 12 LYS B 71 MET B 75 5 5
HELIX 13 13 THR B 76 ASP B 94 1 19
HELIX 14 14 GLN B 107 TYR B 119 1 13
HELIX 15 15 THR B 134 LEU B 140 1 7
HELIX 16 16 GLY B 167 GLN B 175 1 9
HELIX 17 17 PRO B 177 ALA B 183 1 7
HELIX 18 18 PRO B 202 TYR B 212 1 11
HELIX 19 19 SER B 230 ASN B 245 1 16
SHEET 1 A 8 ALA A 2 ARG A 8 0
SHEET 2 A 8 LEU A 11 GLU A 18 -1 O GLY A 15 N ILE A 4
SHEET 3 A 8 ALA A 56 PHE A 60 -1 O ARG A 59 N THR A 16
SHEET 4 A 8 TYR A 25 PHE A 31 1 N ILE A 30 O VAL A 58
SHEET 5 A 8 VAL A 97 SER A 106 1 O ASN A 99 N MET A 27
SHEET 6 A 8 ILE A 123 PRO A 131 1 O VAL A 127 N LEU A 102
SHEET 7 A 8 VAL A 189 GLY A 194 1 O ILE A 192 N ALA A 130
SHEET 8 A 8 SER A 215 ILE A 220 1 O THR A 216 N LEU A 191
SHEET 1 B 2 ASN A 143 THR A 144 0
SHEET 2 B 2 VAL A 147 THR A 148 -1 O VAL A 147 N THR A 144
SHEET 1 C 2 ARG A 157 PRO A 159 0
SHEET 2 C 2 THR A 164 GLY A 166 -1 O LEU A 165 N LEU A 158
SHEET 1 D 8 THR B 3 ARG B 8 0
SHEET 2 D 8 LEU B 11 GLU B 18 -1 O GLY B 15 N ILE B 4
SHEET 3 D 8 ILE B 55 PHE B 60 -1 O SER B 57 N GLU B 18
SHEET 4 D 8 TYR B 25 PHE B 31 1 N ASP B 26 O ALA B 56
SHEET 5 D 8 VAL B 97 SER B 106 1 O VAL B 103 N PHE B 31
SHEET 6 D 8 ILE B 123 PRO B 131 1 O LYS B 124 N ILE B 100
SHEET 7 D 8 VAL B 189 GLY B 194 1 O CYS B 190 N LEU B 128
SHEET 8 D 8 SER B 215 ILE B 220 1 O THR B 216 N LEU B 191
SHEET 1 E 2 ASN B 143 THR B 144 0
SHEET 2 E 2 VAL B 147 THR B 148 -1 O VAL B 147 N THR B 144
SHEET 1 F 2 ARG B 157 PHE B 160 0
SHEET 2 F 2 LEU B 163 GLY B 166 -1 O LEU B 165 N LEU B 158
LINK NA NA B 251 O HOH B 279 1555 1555 2.35
LINK NA NA B 250 O HOH B 268 1555 1555 2.56
SITE 1 AC1 1 LEU A 78
SITE 1 AC2 2 PRO B 95 HOH B 268
SITE 1 AC3 3 LYS A 161 ALA B 2 HOH B 279
CRYST1 149.899 149.899 130.309 90.00 90.00 120.00 H 3 2 36
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006671 0.003852 0.000000 0.00000
SCALE2 0.000000 0.007703 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007674 0.00000
TER 1938 ASN A 245
TER 3838 ASN B 245
MASTER 487 0 3 19 24 0 3 6 3985 2 4 42
END |